Fig. 4: Interactions between MmpL5 and AcpM.
From: Structure and assembly of the MmpL5/MmpS5 efflux transporter from Mycobacterium tuberculosis
a Structure of MmpL5 bound AcpM represented in cartoon and surface. 4′-phosphopantetheine (Ppant) covalently linked to AcpM is shown as red sticks. b, c Close-up views of the binding site between MmpL5 and AcpM. Key residues are shown as stick models. Hydrogen bonds and salt bridges are represented by black dashed lines. d Superposition of M. smegmatis AcpM (pink) and M. tuberculosis MbtL (Alphafold 2 model, light green). Ppant and the modified residue (Ser41) of AcpM are shown as stick models with the electron density displayed as mesh at a 0.2 σ threshold. e Sequence alignment of AcpM and MbtL from M. smegmatis and M. tuberculosis. Contacting residues at the interface are marked by yellow spheres.
